Protein Family Models

This domain is found in formate dehydrogenase H for which the structure is known. This first domain (residues 1 to 60) of PDB:1aa6 is an Fe4S4 cluster just below the protein surface [1]. [1]. 9036855. Crystal structure of formate dehydrogenase H: catalysis. involving Mo, molybdopterin, selenocysteine, and an Fe4S4. cluster.. Boyington JC, Gladyshev VN, Khangulov SV, Stadtman TC, Sun PD;. Science. 1997;275:1305-1308. (from Pfam)

Date:

2024-08-14

This domain is found in various molybdopterin - containing oxidoreductases and tungsten formylmethanofuran dehydrogenase subunit d (FwdD) and molybdenum formylmethanofuran dehydrogenase subunit (FmdD); where the domain constitutes almost the entire subunit. The formylmethanofuran dehydrogenase catalyses the first step in methane formation from CO2 in methanogenic archaea and has a molybdopterin dinucleotide cofactor [1]. This domain corresponds to the C-terminal domain IV in dimethyl sulfoxide (DMSO)reductase which interacts with the 2-amino pyrimidone ring of both molybdopterin guanine dinucleotide molecules [2]. [1]. 9818358. The formylmethanofuran dehydrogenase isoenzymes in. Methanobacterium wolfei and Methanobacterium. thermoautotrophicum: induction of the molybdenum isoenzyme by. molybdate and constitutive synthesis of the tungsten isoenzyme.. Hochheimer A, Hedderich R, Thauer RK;. Arch Microbiol 1998;170:389-393.. [2]. 8890912. Crystal structure of dimethyl sulfoxide reductase from. Rhodobacter capsulatus at 1.88 A resolution.. Schneider F, Lowe J, Huber R, Schindelin H, Kisker C, Knablein. J;. J Mol Biol 1996;263:53-69. (from Pfam)

Date:

2024-08-14

Date:

2024-08-14

nitrate reductase catalyzes the reduction of nitrate into nitrite using a mononuclear molybdenum cofactor

Date:

2017-02-03

With NapBC catalyzes the reduction of nitrate to nitrite; NapAB receives electrons from NapC

Gene:

napA

Date:

2021-08-31

This model represents the large subunit of a family of nitrate reductases found in proteobacteria which are localized to the periplasm. This subunit binds molybdopterin and contains a twin-arginine motif at the N-terminus. The protein associates with NapB, a soluble heme-containing protein and NapC, a membrane-bound cytochrome c. The periplasmic nitrate reductases are not involved in the assimilation of nitrogen, and are not directly involved in the formation of electrochemical gradients (i.e. respiration) either. Rather, the purpose of this enzyme is either dissimilatory (i.e. to dispose of excess reductive equivalents) or indirectly respiratory by virtue of the consumption of electrons derived from NADH via the proton translocating NADH dehydrogenase [4]. The enzymes from Alicagenes eutrophus [1] and Paracoccus pantotrophus [2] have been characterized. In E. coli [3] (as well as other organisms) this gene is part of a large nitrate reduction operon (napFDAGHBC).

Gene:

napA

Date:

2024-06-24